pbscie3 m3

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Proteins are considered asthe most abundant molecules BEFORE water. They occur as unbranched polymer in which the monomer units are amino acids.

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non-polar amino acids examples are alanine and tryptophan. They are generally found in the INTERIOR of proteins(devoid of water).

methionine and phenylalanine are examples of polar but neutral amino acids.

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Polar basic amino acids contain one amino group and two carboxyl group. Polar acidic amino acids contain two amino group and one carboxyl group.

side chain of polar acidic amino acid bears a negative charge

side chain of polar acidic amino acid bears a positive charge

arginine is required for the growth of children and also essential for adults

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all standard amino acid are ACHIRAL. Except Glycerin which is the simplest of the standard amino acids, is CHIRAL

A molecule that has a +charge on one atom and a -charge on another atom, but has no net charge

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isoelecticpoint is the pH at whcih an amino acid exists primarily. At isoelectricpoint almost all amino acid molecules in a solution are present in their zwitterion form

a covalent bond between the carboxyl group of one amino acid and the amino acid gr. of another amino acid

regulates uterine contractions and lactations
stimulates the flow of milk in a nursing mother

regulates the secretion of water
can also affect blood pressure

are pentapeptide neurotransmitters
help reduce pain

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Glutathione is a tripeptide present in LOW levels in most cells. It is the regulator of oxidation and reduction reactions.

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Glutathione is an antioxidant and also protects contents from oxidizing agents. Whitening is one of its side effects.

Protein is a peptide in which at least 40 amino acid residues are present

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MONOMERIC protein contains one peptide chain. MULTIMERIC protein contains more than one peptide chain.

Based on chemical composition, a simple protein contain one amino acid and one non amnino acid residue, while conjugated proteins contian one or more non-amino acid entity to one or more peptide chains.

STRUCTURE OF PROTEINS

ORDER in which amino acid are linked together in a protein

STRUCTURE OF PROTEINS

ORDER of attachment to each other (peptides)

STRUCTURE OF PROTIENS

Arrangement in SPACE adpoted by the backbone portion of a protein

PROTEIN SECONDARY STRUCTURE

single protein chain adopts a shape that resembles a coiled spring maintianed by H-bonds

SECONDARY STRUCTURE PROTEINS

Two fully extended protein chain segments in the same or different molecules are together by H-bonds

SECONDARY STRUCTURE PROTEINS

either be INTRAMOLECULAR or INTERMOLECULAR

SECONDARY STRUCTURE PROTEINS

only INTRAMOLECULAR

STRUCTURE OF PROTIENS

overall 3D shape of protein due to the interactions of amino acid side-chains that are widely separated from each other.

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GLOBULAR PROTEINS have spherical shape and are water-insoluble. They can undergo denaturation.

function as enzymes and intracellular signaling molecules. EX: hemoglobin and myoglobin

GLOBULAR PROTEINS

regulatory hormone for controlling glucose metabolism

GLOBULAR PROTEINS

Oxygen storage in your muscles

GLOBULAR PROTEINS

transport of iron in blood

GLOBULAR PROTEINS

involved in immune system response

structure of protein (globular, fibrous, etc) that provide support and external protection

structure of protein (globular, fibrous, etc) that hve the tendency to aggregate to form macromolecular structures

structure of protein that have simple, regular, and linear structure

FRIBROUS PROTEIN

most abundant protein in the HUMAN BODY

FIBROUS PROTEIN

ORGANIC COMPONENT OF BONES AND TEETH

FIBROUS PROTEINS

found in SKIN, HAIR, WOOL, HORNS, AND FINGERNAILS

FIBROUS PROTEIN

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KERATIN provides protective coating for organs. COLLAGEN is mainly composed of hydrophobic amino acids.

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FIBRIN is AKA Beta-keratin. SILK FIBROIN is found in blood clots.

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MYOSINS are found in muscle tissue. ELASTINS are found in blood vessels and ligaments

FUNCTIONS

ENZYMES

FUNCTION

IMMUNOGLOBULINS

FUNCTION

FERRETIN AND MYOGLOBIN

FUNCTIONS

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COLLAGEN and KERATIN are nutrient proteins. CASEIN and OVALBUMIN are structural proteins.

FUNCTION

ALBUMIN AND GLOBULIN